The domain within your query sequence starts at position 129 and ends at position 220; the E-value for the A2M_N domain shown below is 1.5e-16.

SVLIQTDKAFYKPKQEVKFRVLTLCSDLKPYRTSVDIFIKDPKSNVIQQWFSQKGDLGVV
SKTFQLSSNPIFGDWSIQVQVNDQQYYQSFQV

A2M_N

A2M_N
PFAM accession number:PF01835
Interpro abstract (IPR002890):

The proteinase-binding alpha-macroglobulins (A2M) [(PUBMED:2473064)] are large glycoproteins found in the plasma of vertebrates, in the hemolymph of some invertebrates and in reptilian and avian egg white. A2M-like proteins are able to inhibit all four classes of proteinases by a 'trapping' mechanism. They have a peptide stretch, called the 'bait region', which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein, thus trapping the proteinase. The entrapped enzyme remains active against low molecular weight substrates, whilst its activity toward larger substrates is greatly reduced, due to steric hindrance. Following cleavage in the bait region, a thiol ester bond, formed between the side chains of a cysteine and a glutamine, is cleaved and mediates the covalent binding of the A2M-like protein to the proteinase.

This entry represents the MG2 (macroglobulin) domain of alpha-2-macroglobulin [(PUBMED:16177781)] and also includes homologous domains found in other proteins.

GO function:endopeptidase inhibitor activity (GO:0004866)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry A2M_N